4 research outputs found
DiffusionVMR: Diffusion Model for Video Moment Retrieval
Video moment retrieval is a fundamental visual-language task that aims to
retrieve target moments from an untrimmed video based on a language query.
Existing methods typically generate numerous proposals manually or via
generative networks in advance as the support set for retrieval, which is not
only inflexible but also time-consuming. Inspired by the success of diffusion
models on object detection, this work aims at reformulating video moment
retrieval as a denoising generation process to get rid of the inflexible and
time-consuming proposal generation. To this end, we propose a novel
proposal-free framework, namely DiffusionVMR, which directly samples random
spans from noise as candidates and introduces denoising learning to ground
target moments. During training, Gaussian noise is added to the real moments,
and the model is trained to learn how to reverse this process. In inference, a
set of time spans is progressively refined from the initial noise to the final
output. Notably, the training and inference of DiffusionVMR are decoupled, and
an arbitrary number of random spans can be used in inference without being
consistent with the training phase. Extensive experiments conducted on three
widely-used benchmarks (i.e., QVHighlight, Charades-STA, and TACoS) demonstrate
the effectiveness of the proposed DiffusionVMR by comparing it with
state-of-the-art methods
K<sub>2</sub>Sr<sub>4</sub>(PO<sub>3</sub>)<sub>10</sub>: A Polyphosphate with Deep-UV Cutoff Edge and Enlarged Birefringence
A new
polyphosphate K2Sr4(PO3)10 is synthesized by a high-temperature solution method. This
compound crystallizes in the triclinic space group of P1Ì…, consisting of
the 1D infinite [PO3]∞ chains and K and
Sr ions between the chains. Compared with AM2(PO3)5 (A = K, Rb, Cs; M = Ba, Pb), K2Sr4(PO3)10 exhibits a more complex [PO3]∞ chain structure and more diverse metal cationic
coordination environment. More importantly, K2Sr4(PO3)10 has both a deep-UV cutoff edge (<200
nm) and a significantly enlarged birefringence. First-principles calculations
indicate that the birefringence of K2Sr4(PO3)10 is 0.017 at 1064 nm, about 2 times that of
RbBa2(PO3)5 (0.008 at 1064 nm), which
reaches a new height among the reported mixed alkali metal and alkaline
earth metal phosphate. Theoretical calculations and structural analyses
show that the enlarged birefringence of K2Sr4(PO3)10 mainly originates from the [PO3]∞ chains arranged in an inverted zigzag.
This discovery introduces a new strategy for devising novel phosphate
deep-UV optical crystals with a large birefringence
Peptide Self-Assemblies from Unusual α‑Sheet Conformations Based on Alternation of d/l Amino Acids
Peptide
self-assembly is a hierarchical process during which secondary
structures formed in the initial stages play a critical role in determining
the subsequent assembling processes and final structural ordering.
Unusual secondary structures hold promise as a source to develop novel
supramolecular architectures with unique properties. In this work,
we report the design of a new peptide self-assembly strategy based
on unusual α-sheet secondary structures. In light of the strong
propensity of leucine toward forming helical conformations and its
high hydrophobicity, we design two short amphiphilic peptides Ac-LDLLDLK-NH2 and Ac-DLLDLLDK-NH2 with alternating l- and d-form amino acids. Microscopic imaging, neutron
scattering, and spectroscopic measurements indicate that the two heterochiral
peptides form highly ordered wide nanotubes and helical ribbons with
monolayer thickness, in sharp contrast to twisted nanofibrils formed
by the homochiral peptide Ac-LLLLK-NH2. Molecular dynamics
simulations from monomers to trimers reveal that the two heteropeptides
fold into α-sheets instead of β-sheets, which readily
pack into tubular architectures in oligomer simulations. Simulated
circular dichroism spectra based on α-sheet oligomers validate
the proposed α-sheet secondary structures. These results form
an important basis for the rational design of higher-order peptide
assemblies with novel properties based on unusual α-sheet secondary
structures